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SOX15_HUMAN
ID   SOX15_HUMAN             Reviewed;         233 AA.
AC   O60248; B4DWU7; D3DTQ0; P35717; Q9Y6W7;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 183.
DE   RecName: Full=Protein SOX-15;
DE   AltName: Full=Protein SOX-12;
DE   AltName: Full=Protein SOX-20;
GN   Name=SOX15; Synonyms=SOX12, SOX20, SOX26, SOX27;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=9540826; DOI=10.1016/s0167-4781(97)00186-3;
RA   Hiraoka Y., Ogawa M., Sakai Y., Taniguchi K., Fujii T., Umezawa A.,
RA   Hata J., Aiso S.;
RT   "Isolation and expression of a human SRY-related cDNA hSOX20.";
RL   Biochim. Biophys. Acta 1396:132-137(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Esophagus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE OF 1-178, AND TISSUE SPECIFICITY.
RC   TISSUE=Fetal brain;
RX   PubMed=8978787; DOI=10.1159/000134200;
RA   Meyer J., Wirth J., Held M., Schempp W., Scherer G.;
RT   "SOX20, a new member of the SOX gene family, is located on chromosome
RT   17p13.";
RL   Cytogenet. Cell Genet. 72:246-249(1996).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 57-115.
RX   PubMed=8332506; DOI=10.1093/nar/21.12.2943;
RA   Goze C., Poulat F., Berta P.;
RT   "Partial cloning of SOX-11 and SOX-12, two new human SOX genes.";
RL   Nucleic Acids Res. 21:2943-2943(1993).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 92-233 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9880678; DOI=10.1007/s003359900925;
RA   Vujic M., Rajic T., Goodfellow P.N., Stevanovic M.;
RT   "cDNA characterization and high resolution mapping of the human SOX20
RT   gene.";
RL   Mamm. Genome 9:1059-1061(1998).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 179-233.
RA   Miyashita A., Shimizu N., Odani S., Nakajima T., Kuwano R.;
RT   "Human SL15 gene, 3'UTR and SOX 20 gene, partial cds.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
CC   -!- FUNCTION: Transcription factor that binds to DNA at the 5'-AACAATG-3'
CC       consensus sequence (By similarity). Acts as a transcriptional activator
CC       and repressor (By similarity). Binds synergistically with POU5F1
CC       (OCT3/4) to gene promoters (By similarity). Binds to the FOXK1 promoter
CC       and recruits FHL3, resulting in transcriptional activation of FOXK1
CC       which leads to myoblast proliferation (By similarity). Acts as an
CC       inhibitor of myoblast differentiation via transcriptional repression
CC       which leads to down-regulation of the muscle-specific genes MYOD and
CC       MYOG (By similarity). Involved in trophoblast giant cell
CC       differentiation via enhancement of HAND1 transcriptional activity (By
CC       similarity). Regulates transcription of HRC via binding to it proximal
CC       enhancer region (By similarity). Involved in skeletal muscle
CC       regeneration (By similarity). Also plays a role in the development of
CC       myogenic precursor cells (By similarity).
CC       {ECO:0000250|UniProtKB:P43267}.
CC   -!- SUBUNIT: Interacts with HAND1; the interaction enhances HAND1-induced
CC       differentiation of trophoblast giant cells (By similarity). Interacts
CC       with POU5F1 (OCT3/4); binds synergistically with POU5F1 to DNA (By
CC       similarity). Interacts with FHL3; the interaction recruits the
CC       transcriptional coactivator FHL3 to the FOXK1 promoter (By similarity).
CC       {ECO:0000250|UniProtKB:P43267}.
CC   -!- INTERACTION:
CC       O60248; O14503: BHLHE40; NbExp=3; IntAct=EBI-5452954, EBI-711810;
CC       O60248; Q96LI6: HSFY2; NbExp=3; IntAct=EBI-5452954, EBI-3957665;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O60248-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O60248-2; Sequence=VSP_056668;
CC   -!- TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues
CC       examined, highest level found in fetal spinal cord and adult brain and
CC       testis. {ECO:0000269|PubMed:8978787, ECO:0000269|PubMed:9880678}.
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DR   EMBL; AB006867; BAA25663.1; -; mRNA.
DR   EMBL; AK301687; BAG63159.1; -; mRNA.
DR   EMBL; AC016876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471108; EAW90156.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90157.1; -; Genomic_DNA.
DR   EMBL; BC000985; AAH00985.1; -; mRNA.
DR   EMBL; BC072003; AAH72003.1; -; mRNA.
DR   EMBL; X73039; CAA51520.1; -; Genomic_DNA.
DR   EMBL; AJ006222; CAA06920.1; -; mRNA.
DR   EMBL; AB025355; BAA78784.1; -; Genomic_DNA.
DR   CCDS; CCDS32549.1; -. [O60248-1]
DR   PIR; S34119; S34119.
DR   RefSeq; NP_008873.1; NM_006942.1. [O60248-1]
DR   AlphaFoldDB; O60248; -.
DR   SMR; O60248; -.
DR   BioGRID; 112548; 131.
DR   IntAct; O60248; 128.
DR   STRING; 9606.ENSP00000355354; -.
DR   iPTMnet; O60248; -.
DR   PhosphoSitePlus; O60248; -.
DR   BioMuta; SOX15; -.
DR   EPD; O60248; -.
DR   MassIVE; O60248; -.
DR   MaxQB; O60248; -.
DR   PaxDb; O60248; -.
DR   PeptideAtlas; O60248; -.
DR   PRIDE; O60248; -.
DR   ProteomicsDB; 49282; -. [O60248-1]
DR   ProteomicsDB; 5383; -.
DR   Antibodypedia; 12118; 199 antibodies from 33 providers.
DR   DNASU; 6665; -.
DR   Ensembl; ENST00000250055.3; ENSP00000355354.2; ENSG00000129194.8. [O60248-1]
DR   Ensembl; ENST00000538513.6; ENSP00000439311.2; ENSG00000129194.8. [O60248-1]
DR   Ensembl; ENST00000570788.1; ENSP00000458286.1; ENSG00000129194.8. [O60248-2]
DR   GeneID; 6665; -.
DR   KEGG; hsa:6665; -.
DR   MANE-Select; ENST00000250055.3; ENSP00000355354.2; NM_006942.2; NP_008873.1.
DR   UCSC; uc002ghy.2; human. [O60248-1]
DR   CTD; 6665; -.
DR   DisGeNET; 6665; -.
DR   GeneCards; SOX15; -.
DR   HGNC; HGNC:11196; SOX15.
DR   HPA; ENSG00000129194; Tissue enhanced (esophagus, skin).
DR   MIM; 601297; gene.
DR   neXtProt; NX_O60248; -.
DR   OpenTargets; ENSG00000129194; -.
DR   PharmGKB; PA36033; -.
DR   VEuPathDB; HostDB:ENSG00000129194; -.
DR   eggNOG; KOG0527; Eukaryota.
DR   GeneTree; ENSGT00940000162099; -.
DR   HOGENOM; CLU_106341_0_0_1; -.
DR   InParanoid; O60248; -.
DR   OMA; GYGSSHC; -.
DR   OrthoDB; 369754at2759; -.
DR   PhylomeDB; O60248; -.
DR   TreeFam; TF351735; -.
DR   PathwayCommons; O60248; -.
DR   SignaLink; O60248; -.
DR   BioGRID-ORCS; 6665; 36 hits in 1089 CRISPR screens.
DR   ChiTaRS; SOX15; human.
DR   GeneWiki; SOX15; -.
DR   GenomeRNAi; 6665; -.
DR   Pharos; O60248; Tbio.
DR   PRO; PR:O60248; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; O60248; protein.
DR   Bgee; ENSG00000129194; Expressed in lower esophagus mucosa and 154 other tissues.
DR   Genevisible; O60248; HS.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR   GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0006325; P:chromatin organization; NAS:UniProtKB.
DR   GO; GO:0008584; P:male gonad development; TAS:ProtInc.
DR   GO; GO:0048627; P:myoblast development; ISS:BHF-UCL.
DR   GO; GO:0045843; P:negative regulation of striated muscle tissue development; ISS:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR   GO; GO:0070318; P:positive regulation of G0 to G1 transition; ISS:BHF-UCL.
DR   GO; GO:2000288; P:positive regulation of myoblast proliferation; ISS:BHF-UCL.
DR   GO; GO:0014718; P:positive regulation of satellite cell activation involved in skeletal muscle regeneration; ISS:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl.
DR   GO; GO:0060707; P:trophoblast giant cell differentiation; ISS:UniProtKB.
DR   Gene3D; 1.10.30.10; -; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR031269; SOX15.
DR   PANTHER; PTHR10270:SF45; PTHR10270:SF45; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..233
FT                   /note="Protein SOX-15"
FT                   /id="PRO_0000048762"
FT   DNA_BIND        49..117
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1..47
FT                   /note="Required to promote HAND1 transcriptional activator
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P43267"
FT   REGION          113..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..183
FT                   /note="Interaction with FHL3"
FT                   /evidence="ECO:0000250|UniProtKB:P43267"
FT   REGION          208..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..225
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   VAR_SEQ         179..233
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056668"
FT   CONFLICT        25..27
FT                   /note="SSS -> AAA (in Ref. 6)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69..70
FT                   /note="QQ -> HE (in Ref. 7; CAA51520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191
FT                   /note="S -> F (in Ref. 9; BAA78784)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216..218
FT                   /note="PTP -> STS (in Ref. 9; BAA78784)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225..226
FT                   /note="GA -> VP (in Ref. 9; BAA78784)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   233 AA;  25251 MW;  6B52AE455C7C8CCE CRC64;
     MALPGSSQDQ AWSLEPPAAT AAASSSSGPQ EREGAGSPAA PGTLPLEKVK RPMNAFMVWS
     SAQRRQMAQQ NPKMHNSEIS KRLGAQWKLL DEDEKRPFVE EAKRLRARHL RDYPDYKYRP
     RRKAKSSGAG PSRCGQGRGN LASGGPLWGP GYATTQPSRG FGYRPPSYST AYLPGSYGSS
     HCKLEAPSPC SLPQSDPRLQ GELLPTYTHY LPPGSPTPYN PPLAGAPMPL THL
 
 
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